JPH02194A - ヒト血清アルブミンのn‐未端を含有するポリペプチド - Google Patents
ヒト血清アルブミンのn‐未端を含有するポリペプチドInfo
- Publication number
- JPH02194A JPH02194A JP63272005A JP27200588A JPH02194A JP H02194 A JPH02194 A JP H02194A JP 63272005 A JP63272005 A JP 63272005A JP 27200588 A JP27200588 A JP 27200588A JP H02194 A JPH02194 A JP H02194A
- Authority
- JP
- Japan
- Prior art keywords
- hsa
- nucleotide sequence
- polypeptide
- serum albumin
- human serum
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
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- CDAISMWEOUEBRE-GPIVLXJGSA-N inositol Chemical compound O[C@H]1[C@H](O)[C@@H](O)[C@H](O)[C@H](O)[C@@H]1O CDAISMWEOUEBRE-GPIVLXJGSA-N 0.000 description 1
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- 208000017169 kidney disease Diseases 0.000 description 1
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- 239000003550 marker Substances 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 229960003512 nicotinic acid Drugs 0.000 description 1
- 235000001968 nicotinic acid Nutrition 0.000 description 1
- 239000011664 nicotinic acid Substances 0.000 description 1
- 231100000252 nontoxic Toxicity 0.000 description 1
- 230000003000 nontoxic effect Effects 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 229940111202 pepsin Drugs 0.000 description 1
- 235000019319 peptone Nutrition 0.000 description 1
- 230000000144 pharmacologic effect Effects 0.000 description 1
- PTMHPRAIXMAOOB-UHFFFAOYSA-L phosphoramidate Chemical compound NP([O-])([O-])=O PTMHPRAIXMAOOB-UHFFFAOYSA-L 0.000 description 1
- 230000036470 plasma concentration Effects 0.000 description 1
- 231100000614 poison Toxicity 0.000 description 1
- 102000054765 polymorphisms of proteins Human genes 0.000 description 1
- 229910001414 potassium ion Inorganic materials 0.000 description 1
- 235000008160 pyridoxine Nutrition 0.000 description 1
- 239000011677 pyridoxine Substances 0.000 description 1
- 230000010076 replication Effects 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- CDAISMWEOUEBRE-UHFFFAOYSA-N scyllo-inosotol Natural products OC1C(O)C(O)C(O)C(O)C1O CDAISMWEOUEBRE-UHFFFAOYSA-N 0.000 description 1
- 230000003248 secreting effect Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 150000003384 small molecules Chemical class 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229960005480 sodium caprylate Drugs 0.000 description 1
- 229910001415 sodium ion Inorganic materials 0.000 description 1
- BYKRNSHANADUFY-UHFFFAOYSA-M sodium octanoate Chemical compound [Na+].CCCCCCCC([O-])=O BYKRNSHANADUFY-UHFFFAOYSA-M 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
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- 229940124597 therapeutic agent Drugs 0.000 description 1
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- 235000019157 thiamine Nutrition 0.000 description 1
- 239000011721 thiamine Substances 0.000 description 1
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- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
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Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/76—Albumins
- C07K14/765—Serum albumin, e.g. HSA
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P11/00—Drugs for disorders of the respiratory system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P17/00—Drugs for dermatological disorders
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P9/00—Drugs for disorders of the cardiovascular system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- General Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Biochemistry (AREA)
- Gastroenterology & Hepatology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Molecular Biology (AREA)
- Genetics & Genomics (AREA)
- Biophysics (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Dermatology (AREA)
- Diabetes (AREA)
- Hematology (AREA)
- Pulmonology (AREA)
- Heart & Thoracic Surgery (AREA)
- Cardiology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Materials For Medical Uses (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| GB8725529 | 1987-10-30 | ||
| GB878725529A GB8725529D0 (en) | 1987-10-30 | 1987-10-30 | Polypeptides |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH02194A true JPH02194A (ja) | 1990-01-05 |
Family
ID=10626211
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP63272005A Pending JPH02194A (ja) | 1987-10-30 | 1988-10-29 | ヒト血清アルブミンのn‐未端を含有するポリペプチド |
Country Status (17)
| Country | Link |
|---|---|
| US (1) | US5380712A (fr) |
| EP (1) | EP0322094B1 (fr) |
| JP (1) | JPH02194A (fr) |
| KR (1) | KR0153516B1 (fr) |
| AT (1) | ATE82858T1 (fr) |
| AU (1) | AU619768B2 (fr) |
| CA (1) | CA1341298C (fr) |
| DE (1) | DE3876401T2 (fr) |
| DK (1) | DK175046B1 (fr) |
| ES (1) | ES2053758T3 (fr) |
| FI (1) | FI101381B1 (fr) |
| GB (1) | GB8725529D0 (fr) |
| GR (1) | GR3007162T3 (fr) |
| HU (1) | HU209145B (fr) |
| IE (1) | IE61050B1 (fr) |
| IL (1) | IL88223A (fr) |
| ZA (1) | ZA888118B (fr) |
Families Citing this family (176)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6406697B1 (en) | 1989-02-23 | 2002-06-18 | Genentech, Inc. | Hybrid immunoglobulins |
| US5225538A (en) * | 1989-02-23 | 1993-07-06 | Genentech, Inc. | Lymphocyte homing receptor/immunoglobulin fusion proteins |
| US5116964A (en) * | 1989-02-23 | 1992-05-26 | Genentech, Inc. | Hybrid immunoglobulins |
| GB8909916D0 (en) * | 1989-04-29 | 1989-06-14 | Delta Biotechnology Ltd | Polypeptides |
| US5766883A (en) * | 1989-04-29 | 1998-06-16 | Delta Biotechnology Limited | Polypeptides |
| ATE92107T1 (de) * | 1989-04-29 | 1993-08-15 | Delta Biotechnology Ltd | N-terminale fragmente von menschliches serumalbumin enthaltenden fusionsproteinen. |
| GB8927480D0 (en) * | 1989-12-05 | 1990-02-07 | Delta Biotechnology Ltd | Mutant fungal strain detection and new promoter |
| US5993805A (en) | 1991-04-10 | 1999-11-30 | Quadrant Healthcare (Uk) Limited | Spray-dried microparticles and their use as therapeutic vehicles |
| FR2686899B1 (fr) | 1992-01-31 | 1995-09-01 | Rhone Poulenc Rorer Sa | Nouveaux polypeptides biologiquement actifs, leur preparation et compositions pharmaceutiques les contenant. |
| US5698517A (en) * | 1994-03-21 | 1997-12-16 | University Of Hawaii, Office Of Technology Transfer And Economic Development | Thyroxin-binding HSA fragments |
| DE4436352A1 (de) * | 1994-10-12 | 1996-04-18 | Kay Brune | Verfahren zur diagnostischen Beurteilung und Verlaufskontrolle sowie Arzneimittel zur Therapie von Schockzuständen beim Menschen |
| US5674842A (en) * | 1994-10-26 | 1997-10-07 | Health Research, Incorporated | Growth inhibitory peptide |
| US7597886B2 (en) | 1994-11-07 | 2009-10-06 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US7820798B2 (en) | 1994-11-07 | 2010-10-26 | Human Genome Sciences, Inc. | Tumor necrosis factor-gamma |
| US5723125A (en) * | 1995-12-28 | 1998-03-03 | Tanox Biosystems, Inc. | Hybrid with interferon-alpha and an immunoglobulin Fc linked through a non-immunogenic peptide |
| GB9526733D0 (en) | 1995-12-30 | 1996-02-28 | Delta Biotechnology Ltd | Fusion proteins |
| US7888466B2 (en) | 1996-01-11 | 2011-02-15 | Human Genome Sciences, Inc. | Human G-protein chemokine receptor HSATU68 |
| WO1998006822A1 (fr) * | 1996-08-08 | 1998-02-19 | Yoshitomi Pharmaceutical Industries, Ltd. | Milieu de culture et ses applications |
| US6274305B1 (en) | 1996-12-19 | 2001-08-14 | Tufts University | Inhibiting proliferation of cancer cells |
| GB9815909D0 (en) | 1998-07-21 | 1998-09-16 | Btg Int Ltd | Antibody preparation |
| BR9914519A (pt) * | 1998-10-13 | 2001-07-03 | Univ Georgia Res Found | Peptìdios bioativos estabilizados e métodos de identificação, sìntese e uso |
| US20030190740A1 (en) * | 1998-10-13 | 2003-10-09 | The University Of Georgia Research Foundation, Inc | Stabilized bioactive peptides and methods of identification, synthesis, and use |
| US20050100991A1 (en) * | 2001-04-12 | 2005-05-12 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US6946134B1 (en) | 2000-04-12 | 2005-09-20 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| JP2003530838A (ja) | 2000-04-12 | 2003-10-21 | ヒューマン ゲノム サイエンシズ インコーポレイテッド | アルブミン融合タンパク質 |
| US20030031675A1 (en) | 2000-06-06 | 2003-02-13 | Mikesell Glen E. | B7-related nucleic acids and polypeptides useful for immunomodulation |
| DE60143798D1 (de) | 2000-06-16 | 2011-02-17 | Cambridge Antibody Tech | Immunspezifisch bindende antikörper gegen blys |
| CA2421751C (fr) * | 2000-09-11 | 2014-02-11 | Donald W. Kufe | Domaine extracellulaire du muc1 et compositions et procedes pour le traitement du cancer derives de celui-ci |
| UA93662C2 (uk) | 2000-12-07 | 2011-03-10 | Эли Лилли Энд Компани | Гетерологічний пептидильований глюкагон-подібний білок та його застосування для виготовлення лікарського засобу для лікування пацієнтів, що страждають на ожиріння або інсулінонезалежний цукровий діабет |
| WO2002058450A2 (fr) * | 2000-12-22 | 2002-08-01 | Dana-Faber Cancer Institute, Inc. | Regulation de la proliferation cellulaire par muc1 |
| US20050054051A1 (en) * | 2001-04-12 | 2005-03-10 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US7507413B2 (en) | 2001-04-12 | 2009-03-24 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20060084794A1 (en) * | 2001-04-12 | 2006-04-20 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20050244931A1 (en) * | 2001-04-12 | 2005-11-03 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| WO2002083704A1 (fr) | 2001-04-13 | 2002-10-24 | Human Genome Sciences, Inc. | Facteur de croissance 2, endothelial, vasculaire |
| JP4309758B2 (ja) | 2001-05-25 | 2009-08-05 | ヒューマン ジノーム サイエンシーズ, インコーポレイテッド | Trailレセプターに免疫特異的に結合する抗体 |
| WO2003030821A2 (fr) * | 2001-10-05 | 2003-04-17 | Human Genome Sciences, Inc. | Proteines de fusion d'albumine |
| EP2305312B1 (fr) | 2001-10-10 | 2015-03-04 | ratiopharm GmbH | Remodelage et glycoconjugation de l'hormone folliculo-stimulante (FSH) |
| ES2425738T3 (es) | 2001-12-21 | 2013-10-17 | Human Genome Sciences, Inc. | Proteínas de fusión de la albúmina |
| AU2002364587A1 (en) | 2001-12-21 | 2003-07-30 | Human Genome Sciences, Inc. | Albumin fusion proteins |
| US20080194481A1 (en) | 2001-12-21 | 2008-08-14 | Human Genome Sciences, Inc. | Albumin Fusion Proteins |
| KR20110014661A (ko) | 2002-02-07 | 2011-02-11 | 노보자임스 바이오파마 디케이 에이/에스 | 알부민-융합 쿠니츠 도메인 펩타이드 |
| US20060002935A1 (en) | 2002-06-28 | 2006-01-05 | Domantis Limited | Tumor Necrosis Factor Receptor 1 antagonists and methods of use therefor |
| GB0217033D0 (en) | 2002-07-23 | 2002-08-28 | Delta Biotechnology Ltd | Gene and polypeptide sequences |
| WO2004041862A2 (fr) | 2002-11-08 | 2004-05-21 | Ablynx N.V. | Anticorps a domaine unique diriges contre le facteur de necrose tumorale alpha et leurs utilisations |
| EP1594530A4 (fr) | 2003-01-22 | 2006-10-11 | Human Genome Sciences Inc | Proteines hybrides d'albumine |
| EP1615945B1 (fr) | 2003-04-09 | 2011-09-28 | BioGeneriX AG | Methode de glycopegylation et proteines/peptides produits au moyen de ces methodes |
| WO2004092339A2 (fr) * | 2003-04-11 | 2004-10-28 | Ilex Products, Inc. | Modulation de la transduction de signal a mediation muc1 |
| US8129506B2 (en) * | 2003-10-24 | 2012-03-06 | Genzyme Corporation | Modulation of the interaction of MUC1 with MUC1 ligands |
| EP1729795B1 (fr) | 2004-02-09 | 2016-02-03 | Human Genome Sciences, Inc. | Proteines hybrides d'albumine |
| CA2556729A1 (fr) * | 2004-02-23 | 2005-09-09 | Genzyme Corporation | Stimulation de l'apoptose declenchee par le ligand du recepteur de mort par l'antagoniste de muc1 |
| US7973139B2 (en) | 2004-03-26 | 2011-07-05 | Human Genome Sciences, Inc. | Antibodies against nogo receptor |
| US20060204512A1 (en) | 2004-09-23 | 2006-09-14 | Vasgene Therapeutics, Inc. | Polypeptide compounds for inhibiting angiogenesis and tumor growth |
| CN101724071A (zh) | 2004-10-08 | 2010-06-09 | 杜门蒂斯有限公司 | 抗肿瘤坏死因子受体1的单域抗体及其使用方法 |
| NZ597082A (en) | 2005-10-13 | 2013-11-29 | Human Genome Sciences Inc | Methods and Compositions for Use in Treatment of Patients with Autoantibody Positive Diseases |
| EP2054437A2 (fr) | 2006-08-07 | 2009-05-06 | Teva Biopharmaceuticals USA, Inc. | Protéines de fusion d'albumine et d'insuline |
| DK2615108T3 (en) | 2006-09-08 | 2017-01-30 | Ambrx Inc | Modified human plasma polypeptide or fc scaffolds and their applications |
| CA3161849A1 (fr) | 2007-01-30 | 2008-08-07 | Epivax, Inc. | Epitopes de lymphocytes t regulateurs, compositions et utilisations de ceux-ci |
| US7972870B2 (en) | 2007-02-02 | 2011-07-05 | Dana-Farber Cancer Institute, Inc. | Methods and compositions relating to the regulation of MUC1 by HSF1 and STAT3 |
| US7871784B2 (en) * | 2007-02-02 | 2011-01-18 | Dana-Farber Cancer Institute, Inc. | Methods and compositions relating to the regulation of apoptosis by MUC1 and BH3-containing proapoptotic proteins |
| EP2450054B1 (fr) | 2007-04-12 | 2018-07-18 | Stichting Katholieke Universiteit | Nouveaux facteurs de virulence de la pneumonie ?streptocoques |
| AU2008237632B2 (en) | 2007-04-17 | 2014-01-16 | Stichting Dienst Landbouwkundig Onderzoek | Mammalian-type glycosylation in plants by expression of non-mammalian glycosyltransferases |
| EP2076533B1 (fr) | 2007-05-02 | 2014-10-08 | Ambrx, Inc. | Polypeptides d'interferon beta modifies et leurs utilisations |
| EA200901494A1 (ru) | 2007-06-06 | 2010-06-30 | Домантис Лимитед | Способы селекции протеазоустойчивых полипептидов |
| TWI489993B (zh) | 2007-10-12 | 2015-07-01 | Novartis Ag | 骨硬化素(sclerostin)抗體組合物及使用方法 |
| US8946148B2 (en) | 2007-11-20 | 2015-02-03 | Ambrx, Inc. | Modified insulin polypeptides and their uses |
| PL2318029T3 (pl) | 2008-07-23 | 2018-03-30 | Elanco Us Inc. | Zmodyfikowane polipeptydy bydlęcego G-CSF i ich zastosowania |
| EP2174664A1 (fr) | 2008-10-07 | 2010-04-14 | Stichting Katholieke Universiteit, more particularly the Radboud University Nijmegen Medical Centre | Nouveaux facteurs de virulence de la pneumonie à streptocoques |
| IT1392551B1 (it) * | 2008-11-25 | 2012-03-09 | Bioindustry Park Del Canavese S P A | Biomarcatori per la diagnosi e per rilevare la progressione di malattie neurodegenerative, in particolare della sclerosi laterale amiotrofica |
| CN102307897B (zh) | 2008-12-05 | 2016-01-20 | 葛兰素集团有限公司 | 选出蛋白酶抗性多肽的方法 |
| SG172789A1 (en) | 2009-02-11 | 2011-08-29 | Novozymes Biopharma Dk As | Albumin variants and conjugates |
| EP2398827A2 (fr) | 2009-02-19 | 2011-12-28 | Glaxo Group Limited | Polypeptides, domaines variables d'anticorps, et antagonistes améliorés, tous étant des anti-tnfr1 |
| KR20120057563A (ko) | 2009-03-31 | 2012-06-05 | 노파르티스 아게 | Il-12 수용체 베타l 서부유닛에 대해 특이적인 치료용 항체를 사용하는 조성물 및 방법 |
| EA027071B1 (ru) | 2009-04-27 | 2017-06-30 | Новартис Аг | АНТИТЕЛО К ActRIIB И СОДЕРЖАЩАЯ ЕГО КОМПОЗИЦИЯ |
| JP2012532619A (ja) | 2009-07-16 | 2012-12-20 | グラクソ グループ リミテッド | Tnfr1を部分的に阻害するためのアンタゴニスト、用途および方法 |
| WO2011029823A1 (fr) | 2009-09-09 | 2011-03-17 | Novartis Ag | Anticorps monoclonal réactif avec cd63 lors de son expression à la surface de mastocytes dégranulés |
| PE20121564A1 (es) | 2009-10-27 | 2012-11-29 | Glaxo Group Ltd | Polipeptidos anti-tnfr1 estables, dominios variables de anticuerpos y antagonistas |
| BR112012009450A2 (pt) | 2009-10-30 | 2017-05-23 | Novozymes Biopharma Dk As | variantes de albumina |
| GB0919054D0 (en) | 2009-10-30 | 2009-12-16 | Isis Innovation | Treatment of obesity |
| GB0919837D0 (en) | 2009-11-13 | 2009-12-30 | Isis Innovation | Method of treatment and screening method |
| BR112012015461A2 (pt) | 2009-12-21 | 2017-01-10 | Ambrx Inc | polipeptídeos de somatotropina boviina modificados e seus usos |
| US20120283172A1 (en) | 2009-12-21 | 2012-11-08 | Ambrx, Inc. | Modified porcine somatotropin polypeptides and their uses |
| CA2790984C (fr) | 2010-02-23 | 2018-07-17 | Stichting Katholieke Universiteit | Vaccin combine pour streptococcus |
| EP2556087A1 (fr) | 2010-04-09 | 2013-02-13 | Novozymes Biopharma DK A/S | Dérivés et variants d'albumine |
| EP3572091B1 (fr) | 2010-08-17 | 2023-12-13 | Ambrx, Inc. | Polypeptides de relaxine modifiés et leurs utilisations |
| JP2013543384A (ja) | 2010-10-05 | 2013-12-05 | ノバルティス アーゲー | 抗−il12rベータ1抗体ならびに自己免疫性および炎症性疾患の処置おけるその使用 |
| KR20190112175A (ko) | 2010-12-01 | 2019-10-02 | 앨더바이오 홀딩스 엘엘씨 | 항―ngf 조성물 및 그의 용도 |
| AU2012222833B2 (en) | 2011-03-03 | 2017-03-16 | Zymeworks Inc. | Multivalent heteromultimer scaffold design and constructs |
| WO2012156309A1 (fr) | 2011-05-13 | 2012-11-22 | Millegen | Anticorps contre her3 |
| EP3662932B1 (fr) | 2011-05-20 | 2021-04-07 | H. Lundbeck A/S | Compositions anti-cgrp et leur utilisation |
| CN103957935B (zh) | 2011-05-20 | 2018-04-03 | 奥尔德生物控股有限责任公司 | 抗cgrp或抗cgrp‑r抗体或抗体片段用于治疗或预防慢性和急性形式的腹泻的用途 |
| NZ732970A (en) | 2011-05-20 | 2022-08-26 | H Lundbeck As | Use of anti-cgrp antibodies and antibody fragments to prevent or inhibit photophobia or light aversion in subjects in need thereof, especially migraine sufferers |
| WO2012175692A1 (fr) | 2011-06-22 | 2012-12-27 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Anticorps anti-axl et utilisations associées |
| JP6033293B2 (ja) | 2011-06-22 | 2016-11-30 | インサーム(インスティテュ ナシオナル ドゥ ラ サンテ エ ドゥ ラ ルシェルシェ メディカル)Inserm(Institut National Dela Sante Et De La Recherche Medicale) | 抗Axl抗体及びその使用 |
| JP6472999B2 (ja) | 2011-07-01 | 2019-02-20 | ノバルティス アーゲー | 代謝障害を治療するための方法 |
| RU2014103288A (ru) | 2011-07-01 | 2015-08-10 | Байер Интеллектчуал Проперти Гмбх | Слитые полипептиды релаксина и их применение |
| KR20140039257A (ko) | 2011-07-08 | 2014-04-01 | 바이엘 인텔렉쳐 프로퍼티 게엠베하 | 릴랙신을 방출하는 융합 단백질 및 이의 용도 |
| JP6094485B2 (ja) * | 2011-08-10 | 2017-03-15 | ニプロ株式会社 | ビリルビン排泄促進剤 |
| EP2780364A2 (fr) | 2011-11-18 | 2014-09-24 | Eleven Biotherapeutics, Inc. | Protéines ayant une demi-vie et d'autres propriétés améliorées |
| ES2664328T3 (es) | 2012-03-16 | 2018-04-19 | Albumedix A/S | Variantes de albúmina |
| US9745359B2 (en) | 2012-05-18 | 2017-08-29 | Adda Biotech Inc. | Protein and protein conjugate for diabetes treatment, and applications thereof |
| JP6498601B2 (ja) | 2012-07-13 | 2019-04-10 | ザイムワークス,インコーポレイテッド | 多価ヘテロ多量体足場設計および構築物 |
| US9376489B2 (en) | 2012-09-07 | 2016-06-28 | Novartis Ag | IL-18 binding molecules |
| CA2890766A1 (fr) | 2012-11-08 | 2014-05-15 | Novozymes Biopharma Dk A/S | Variants d'albumine |
| SI2953969T1 (sl) | 2013-02-08 | 2020-01-31 | Novartis Ag | Protitelesa proti-IL-17A in njihova uporaba v zdravljenju avtoimunskih in vnetnih motenj |
| EP2968587A2 (fr) | 2013-03-13 | 2016-01-20 | Bristol-Myers Squibb Company | Domaines d'échafaudage à base de fibronectine liés à une sérum albumine ou fragment se liant à celle-ci |
| KR102476907B1 (ko) | 2013-07-03 | 2022-12-13 | 하. 룬드벡 아크티에셀스카브 | 항-cgrp 항체를 사용하는 글루코오스 대사의 조절 |
| EP3033358A2 (fr) | 2013-08-14 | 2016-06-22 | Novartis AG | Traitement de la myosite corps d'inclusion sporadique |
| BR112016010336A2 (pt) | 2013-11-07 | 2017-10-03 | Inst Nat Sante Rech Med | Anticorpo anti-humano-her3 alostérico não competitivo com neuregulina, fragmento de anticorpo, sequência de ácido nucleico, vetor, célula hospedeira, composição farmacêutica e método para tratamento de câncer |
| WO2015081891A1 (fr) | 2013-12-06 | 2015-06-11 | Baikang (Suzhou) Co., Ltd | Pro-fragments bioréversibles pour médicaments contenant de l'azote et de l'hydroxyle |
| JP6865584B2 (ja) * | 2013-12-23 | 2021-04-28 | コヴァラブ | 化合物の共有結合性コンジュゲーションのためのmTG基質 |
| TW201622746A (zh) | 2014-04-24 | 2016-07-01 | 諾華公司 | 改善或加速髖部骨折術後身體復原之方法 |
| US20170204149A1 (en) | 2014-06-23 | 2017-07-20 | Novartis Ag | Hsa-gdf-15 fusion polypeptide and use thereof |
| US20170291939A1 (en) | 2014-06-25 | 2017-10-12 | Novartis Ag | Antibodies specific for il-17a fused to hyaluronan binding peptide tags |
| ES2848376T3 (es) | 2014-11-19 | 2021-08-09 | Axon Neuroscience Se | Anticuerpos de tau humanizados en la enfermedad de Alzheimer |
| ES2764299T3 (es) | 2014-12-09 | 2020-06-02 | Inst Nat Sante Rech Med | Anticuerpos monoclonales humanos contra AXL |
| ES3057010T3 (en) | 2014-12-19 | 2026-02-25 | H Lundbeck As | Humanized anti-acth antibodies and use thereof |
| NL2014148B1 (en) | 2015-01-16 | 2017-01-05 | Univ Erasmus Med Ct Rotterdam | Combination vaccine for camelids. |
| WO2016135041A1 (fr) | 2015-02-26 | 2016-09-01 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Protéines de fusion et anticorps les contenant pour favoriser l'apoptose |
| PL3298140T3 (pl) | 2015-05-19 | 2024-11-12 | Yale University | Kompozycje do leczenia patologicznych stanów zwapnienia i sposoby ich stosowania |
| EP3298044B1 (fr) | 2015-05-22 | 2021-08-25 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Fragments d'anticorps monoclonaux humains pour inhiber à la fois l'activité cath-d catalytique et sa liaison au récepteur lrp1 |
| AU2016303688B2 (en) | 2015-07-31 | 2023-06-15 | Research Institute At Nationwide Children's Hospital | Peptides and antibodies for the removal of biofilms |
| CA2989966C (fr) | 2015-08-20 | 2024-04-30 | Albumedix A/S | Variants de l'albumine et leurs conjugues |
| WO2017066719A2 (fr) | 2015-10-14 | 2017-04-20 | Research Institute At Nationwide Children's Hospital | Agents spécifiques interférant avec hu |
| DK3368571T5 (da) | 2015-10-30 | 2024-09-30 | Univ California | Transformerende, vækstfaktor-beta-responsive polypeptider og fremgangsmåder til anvendelse deraf |
| WO2017109706A1 (fr) | 2015-12-22 | 2017-06-29 | Novartis Ag | Méthodes de traitement ou d'amélioration de troubles métaboliques à l'aide du facteur-15 de croissance et de différenciation (gdf-15) |
| KR102438140B1 (ko) | 2016-03-22 | 2022-08-31 | 엥스띠뛰 나씨오날 드 라 쌍떼 에 드 라 흐쉐르슈 메디깔 | 인간화 항-클라우딘-1 항체 및 이의 용도 |
| CA3020839A1 (fr) | 2016-04-15 | 2017-10-19 | Alder Biopharmaceuticals, Inc. | Anticorps anti-pacap et leurs utilisations |
| JP7219207B2 (ja) | 2016-07-29 | 2023-02-07 | アンスティチュ ナショナル ドゥ ラ サンテ エ ドゥ ラ ルシェルシュ メディカル | 腫瘍関連マクロファージを標的化する抗体及びその使用 |
| KR20190057308A (ko) | 2016-09-02 | 2019-05-28 | 더 리전츠 오브 더 유니버시티 오브 캘리포니아 | 인터류킨-6 수용체 알파-결합 단일 사슬 가변 단편을 포함하는 방법 및 조성물 |
| JP7514621B2 (ja) | 2017-01-04 | 2024-07-11 | リサーチ インスティチュート アット ネイションワイド チルドレンズ ホスピタル | Dnabiiワクチンおよび強化された活性を有する抗体 |
| AU2018206560B9 (en) | 2017-01-04 | 2025-04-03 | Research Institute At Nationwide Children's Hospital | Antibody fragments for the treatment of biofilm-related disorders |
| WO2018158398A1 (fr) | 2017-03-02 | 2018-09-07 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Anticorps présentant une spécificité pour la nectine-4 et leurs utilisations |
| US11746136B2 (en) | 2017-03-15 | 2023-09-05 | Research Institute At Nationwide Children's Hospital | Composition and methods for disruption of bacterial biofilms without accompanying inflammation |
| CN110461359B (zh) | 2017-03-24 | 2025-01-21 | 诺华股份有限公司 | 用于预防和治疗心脏病的方法 |
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| JP2020525421A (ja) | 2017-06-28 | 2020-08-27 | ノバルティス アーゲー | 尿失禁を予防及び治療するための方法 |
| JP7165193B2 (ja) | 2017-11-27 | 2022-11-02 | パーデュー、ファーマ、リミテッド、パートナーシップ | ヒト組織因子を標的とするヒト化抗体 |
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| EP3861021B1 (fr) | 2018-10-05 | 2025-02-12 | Research Institute at Nationwide Children's Hospital | Compositions et procédés pour la dégradation enzymatique de biofilms bactériens |
| WO2020152367A1 (fr) | 2019-01-25 | 2020-07-30 | Ospedale San Raffaele S.R.L. | Inhibiteur de dux4 et ses utilisations |
| JP2022526334A (ja) | 2019-03-25 | 2022-05-24 | アンスティチュ ナショナル ドゥ ラ サンテ エ ドゥ ラ ルシェルシュ メディカル | 新たなタウ種を標的化することによるタウオパチー障害の処置の方法 |
| BR112021024938A2 (pt) | 2019-06-12 | 2022-01-25 | Novartis Ag | Anticorpos de receptor 1 de peptídeo natriurético e métodos de uso |
| CA3145385A1 (fr) | 2019-07-08 | 2021-01-14 | Steven D. Goodman | Compositions d'anticorps pour detruire des biofilms |
| EP4034560A1 (fr) | 2019-09-27 | 2022-08-03 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Anticorps de de substance inhibitrice müllérienne et leurs utilisations |
| WO2021058729A1 (fr) | 2019-09-27 | 2021-04-01 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Anticorps dirigés contre le récepteur de type i d'une substance inhibitrice anti-mullérienne et leurs utilisations |
| TW202128160A (zh) | 2019-10-18 | 2021-08-01 | 美國加利福尼亞大學董事會 | 用於治療病原性血管病症之方法及組合物 |
| WO2021116119A1 (fr) | 2019-12-09 | 2021-06-17 | INSERM (Institut National de la Santé et de la Recherche Médicale) | Anticorps présentant une spécificité pour her4 et leurs utilisations |
| JP7767289B2 (ja) | 2020-01-10 | 2025-11-11 | アンセルム(アンスティチュ ナシオナル ドゥ ラ サンテ エ ドゥ ラ ルシェルシュ メディカル) | Rspo1タンパク質およびその使用 |
| CA3077973A1 (fr) | 2020-04-06 | 2021-10-06 | H. Lundbeck A/S | Traitement du symptome le plus perturbant associe a la migraine au moyen d`anticorps anti-cgrp |
| CN115551553A (zh) | 2020-05-12 | 2022-12-30 | Inserm(法国国家健康医学研究院) | 治疗皮肤t细胞淋巴瘤和tfh起源淋巴瘤的新方法 |
| CA3187283A1 (fr) | 2020-06-29 | 2022-01-06 | Inserm (Institut National De La Sante Et De La Recherche Medicale) | Anticorps a domaine unique anti-proteine s et polypeptides les comprenant |
| US12161777B2 (en) | 2020-07-02 | 2024-12-10 | Davol Inc. | Flowable hemostatic suspension |
| US11739166B2 (en) | 2020-07-02 | 2023-08-29 | Davol Inc. | Reactive polysaccharide-based hemostatic agent |
| US20240052042A1 (en) | 2020-12-14 | 2024-02-15 | Novartis Ag | Reversal binding agents for anti-natriuretic peptide receptor i (npri) antibodies and uses thereof |
| CN116744984A (zh) | 2020-12-28 | 2023-09-12 | 达沃有限公司 | 包含蛋白质和多官能化改性的基于聚乙二醇的交联剂的反应性干粉状止血材料 |
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| IL310154A (en) | 2021-07-15 | 2024-03-01 | Diogenx | Recombinant variants of r-spondin proteins and their use |
| JP2024532143A (ja) | 2021-08-27 | 2024-09-05 | ハー・ルンドベック・アクチエゼルスカベット | 抗cgrp抗体を使用した群発頭痛の治療 |
| IL314828A (en) | 2022-03-11 | 2024-10-01 | Mablink Bioscience | Antibody-drug conjugates and their uses |
| CA3254560A1 (fr) | 2022-03-30 | 2023-10-05 | Novartis Ag | Méthodes de traitement de troubles à l'aide d'anticorps anti-récepteur du peptide natriurétique 1 (npr1) |
| EP4584291A1 (fr) | 2022-09-08 | 2025-07-16 | Institut National de la Santé et de la Recherche Médicale | Anticorps présentant une spécificité pour ltbp2 et leurs utilisations |
| WO2024056668A1 (fr) | 2022-09-12 | 2024-03-21 | Institut National de la Santé et de la Recherche Médicale | Nouveaux anticorps anti-itgb8 et leurs utilisations |
| EP4389762A1 (fr) | 2022-12-23 | 2024-06-26 | Ospedale San Raffaele S.r.l. | Inhibiteurs de l'activité de dux4 et leur utilisation en thérapie. |
| EP4652188A1 (fr) | 2023-01-19 | 2025-11-26 | Diogenx | Variants recombinants de protéines r-spondine et leur utilisation |
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| AU2024245676A1 (en) | 2023-03-30 | 2025-10-09 | 272BIO Limited | Gnrh-binding polypeptides and uses thereof |
| CN121511261A (zh) | 2023-05-17 | 2026-02-10 | 国家健康与医学研究院 | 抗组织蛋白酶-d抗体 |
| EP4477236A1 (fr) | 2023-06-14 | 2024-12-18 | Inatherys | Polythérapie pour le traitement d'une tumeur à l'aide d'un adc comprenant des anticorps anti-cd71 et des mimétiques bh3 |
| AU2024313073A1 (en) | 2023-06-23 | 2026-02-12 | H. Lundbeck A/S | Combinational treatment |
| WO2025012417A1 (fr) | 2023-07-13 | 2025-01-16 | Institut National de la Santé et de la Recherche Médicale | Anticorps à fragments longs anti-neurotensine et anti-neuromédine n et leurs utilisations |
| WO2025224297A1 (fr) | 2024-04-26 | 2025-10-30 | Institut National de la Santé et de la Recherche Médicale | Anticorps ayant une spécificité vis-à-vis de tgfbi et leurs utilisations |
| WO2025242732A1 (fr) | 2024-05-21 | 2025-11-27 | Institut National de la Santé et de la Recherche Médicale | Anticorps pan dirigés contre la protéine de spicule du sars-cov-2 et leurs utilisations à des fins thérapeutiques |
| WO2025257181A1 (fr) | 2024-06-11 | 2025-12-18 | Institut National de la Santé et de la Recherche Médicale | Anticorps ciblant la protéine-43 de liaison à l'adn à réponse trans-active (tdp-43) |
| US20260001942A1 (en) | 2024-06-21 | 2026-01-01 | H. Lundbeck A/S | Treatment of headache disorders and/or psychiatric symptoms using anti-cgrp antibodies, and compositions and methods related thereto |
Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6041487A (ja) * | 1983-04-25 | 1985-03-05 | ジエネンテツク・インコ−ポレイテツド | 酵母発現系でのアルフア因子配列の使用 |
| JPS6229985A (ja) * | 1985-06-17 | 1987-02-07 | ジエネツクス・コ−ポレ−シヨン | クロ−ン化プレプロ−ヒト血清アルブミン遺伝子およびヒト血清アルブミン遺伝子、それらの遺伝子を含むプラスミド、プラスミドにより形質転換された微生物、およびその微生物を用いたプレプロ−ヒト血清アルブミン遺伝子の製造方法 |
Family Cites Families (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| IL66614A (en) * | 1981-08-28 | 1985-09-29 | Genentech Inc | Method of constructing a dna sequence encoding a polypeptide,microbial production of human serum albumin,and pharmaceutical compositions comprising it |
| EP0091527A3 (fr) * | 1981-12-14 | 1984-07-25 | The President And Fellows Of Harvard College | Séquences d'ADN, molécules d'ADN recombinant et procédé de préparation de polypeptides du genre de sérumalbumine humaine |
| JPS6087792A (ja) * | 1983-09-23 | 1985-05-17 | ジェネックス・コーポレイション | 雑種制御領域 |
| GB8510219D0 (en) * | 1985-04-22 | 1985-05-30 | Bass Plc | Isolation of fermentation products |
| GB8615701D0 (en) * | 1986-06-27 | 1986-08-06 | Delta Biotechnology Ltd | Stable gene integration vector |
| GB8620926D0 (en) * | 1986-08-29 | 1986-10-08 | Delta Biotechnology Ltd | Yeast promoter |
-
1987
- 1987-10-30 GB GB878725529A patent/GB8725529D0/en active Pending
-
1988
- 1988-10-18 ZA ZA888118A patent/ZA888118B/xx unknown
- 1988-10-19 AU AU24046/88A patent/AU619768B2/en not_active Expired
- 1988-10-20 CA CA000580789A patent/CA1341298C/fr not_active Expired - Fee Related
- 1988-10-25 DE DE8888310000T patent/DE3876401T2/de not_active Expired - Lifetime
- 1988-10-25 ES ES88310000T patent/ES2053758T3/es not_active Expired - Lifetime
- 1988-10-25 EP EP88310000A patent/EP0322094B1/fr not_active Expired - Lifetime
- 1988-10-25 AT AT88310000T patent/ATE82858T1/de not_active IP Right Cessation
- 1988-10-28 FI FI884993A patent/FI101381B1/fi not_active IP Right Cessation
- 1988-10-28 IL IL8822388A patent/IL88223A/en not_active IP Right Cessation
- 1988-10-28 DK DK198806006A patent/DK175046B1/da not_active IP Right Cessation
- 1988-10-28 HU HU885627A patent/HU209145B/hu unknown
- 1988-10-28 IE IE328088A patent/IE61050B1/en not_active IP Right Cessation
- 1988-10-29 JP JP63272005A patent/JPH02194A/ja active Pending
- 1988-10-31 KR KR1019880014255A patent/KR0153516B1/ko not_active Expired - Lifetime
-
1992
- 1992-02-14 US US07/944,706 patent/US5380712A/en not_active Expired - Lifetime
-
1993
- 1993-02-25 GR GR930400399T patent/GR3007162T3/el unknown
Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6041487A (ja) * | 1983-04-25 | 1985-03-05 | ジエネンテツク・インコ−ポレイテツド | 酵母発現系でのアルフア因子配列の使用 |
| JPS6229985A (ja) * | 1985-06-17 | 1987-02-07 | ジエネツクス・コ−ポレ−シヨン | クロ−ン化プレプロ−ヒト血清アルブミン遺伝子およびヒト血清アルブミン遺伝子、それらの遺伝子を含むプラスミド、プラスミドにより形質転換された微生物、およびその微生物を用いたプレプロ−ヒト血清アルブミン遺伝子の製造方法 |
Also Published As
| Publication number | Publication date |
|---|---|
| DK175046B1 (da) | 2004-05-10 |
| AU2404688A (en) | 1989-05-18 |
| GB8725529D0 (en) | 1987-12-02 |
| HU209145B (en) | 1994-03-28 |
| EP0322094A1 (fr) | 1989-06-28 |
| DK600688A (da) | 1989-06-21 |
| US5380712A (en) | 1995-01-10 |
| KR0153516B1 (ko) | 1998-10-15 |
| ATE82858T1 (de) | 1992-12-15 |
| GR3007162T3 (fr) | 1993-07-30 |
| IE883280L (en) | 1989-04-30 |
| HUT47977A (en) | 1989-04-28 |
| KR890006668A (ko) | 1989-06-15 |
| CA1341298C (fr) | 2001-09-25 |
| IE61050B1 (en) | 1994-09-21 |
| DE3876401D1 (de) | 1993-01-14 |
| IL88223A0 (en) | 1989-06-30 |
| DE3876401T2 (de) | 1993-04-22 |
| FI101381B (fi) | 1998-06-15 |
| FI884993L (fi) | 1989-05-01 |
| AU619768B2 (en) | 1992-02-06 |
| IL88223A (en) | 1994-10-07 |
| FI884993A0 (fi) | 1988-10-28 |
| EP0322094B1 (fr) | 1992-12-02 |
| ZA888118B (en) | 1989-07-26 |
| ES2053758T3 (es) | 1994-08-01 |
| FI101381B1 (fi) | 1998-06-15 |
| DK600688D0 (da) | 1988-10-28 |
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